| Literature DB >> 17055489 |
Ellis van Liempt1, Christine M C Bank, Padmaja Mehta, Juan Jesús Garciá-Vallejo, Ziad S Kawar, Rudolf Geyer, Richard A Alvarez, Richard D Cummings, Yvette van Kooyk, Irma van Die.
Abstract
The dendritic cell specific C-type lectin dendritic cell specific ICAM-3 grabbing non-integrin (DC-SIGN) binds to "self" glycan ligands found on human cells and to "foreign" glycans of bacterial or parasitic pathogens. Here, we investigated the binding properties of DC-SIGN to a large array of potential ligands in a glycan array format. Our data indicate that DC-SIGN binds with K(d)<2muM to a neoglycoconjugate in which Galbeta1-4(Fucalpha1-3)GlcNAc (Le(x)) trisaccharides are expressed multivalently. A lower selective binding was observed to oligomannose-type N-glycans, diantennary N-glycans expressing Le(x) and GalNAcbeta1-4(Fucalpha1-3)GlcNAc (LacdiNAc-fucose), whereas no binding was observed to N-glycans expressing core-fucose linked either alpha1-6 or alpha1-3 to the Asn-linked GlcNAc of N-glycans. These results demonstrate that DC-SIGN is selective in its recognition of specific types of fucosylated glycans and subsets of oligomannose- and complex-type N-glycans.Entities:
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Year: 2006 PMID： 17055489 DOI： 10.1016/j.febslet.2006.10.009
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124